Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner. - Wikidata - wikimedia - TriplyDB

Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.

Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.

http://www.wikidata.org/entity/Q30316581

about

Begomoviral Movement Protein Effects in Human and Plant Cells: Towards New Potential Interaction Partners.

P2860

Q47109632-A01577E4-F6DC-4F8B-9A63-F20F61BFFD88

P2860

Parvulin 17-catalyzed Tubulin Polymerization Is Regulated by Calmodulin in a Calcium-dependent Manner.

http://www.wikidata.org/entity/Q30316581

description

2015 nî lūn-bûn

@nan

2015 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

name

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner.

@ast

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner.

@en

type

label

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner.

@ast

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner.

@en

prefLabel

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner.

@ast

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner.

@en

P1433

Q30316581-AB70A98B-3978-40BD-9C17-8C3D01660D06

P1476

Q30316581-B4F70424-B54B-4421-9C7B-A6816FE45067

P2093

Q30316581-11E7F13B-9DFA-40C5-A959-D7111C9D69B4

Q30316581-21EF1C7A-6800-41AF-BE50-977F95A594F4

Q30316581-3EBF892E-F328-4B9D-A9AC-21502C15DFF9

Q30316581-411EDF42-D819-4522-970B-7FF3F2E2FFB9

Q30316581-42398CAB-D19B-4E54-B53C-FC47054AB161

Q30316581-45D06673-86C4-45D3-A35B-78C06C76792F

Q30316581-737AE162-2357-4EDA-B142-EB9ECDE20C62

Q30316581-97FAD2B0-255C-4B65-BFDC-D01A35822195

Q30316581-98F113AF-2161-4034-9604-4AE917DCEA8F

P2860

Q30316581-0402B48E-F809-45B0-B8C1-47C3A96B6D0A

Q30316581-05EBD78C-57F6-4E9A-8C21-DD6293A4E517

Q30316581-0A3F0FCA-AA75-4547-A839-FA41A566B764

Q30316581-0D5A3A96-1192-488B-B7AD-ACE700B4F8E4

Q30316581-0EC4D04E-A40C-4917-8665-F45835BBF188

Q30316581-26B3DEA4-749B-4785-8626-9E8BBE99F6CE

Q30316581-2EF62801-A393-4E33-83A6-5E7A33AE2AE6

Q30316581-39C39629-E238-4CC8-A92E-03CBAB51ABCA

Q30316581-3AB7575E-D3A7-4BDC-B88D-1C768409A244

Q30316581-3AFABB3F-D46E-4D24-87E3-B97BE18F68ED

P304

Q30316581-761C7A8E-C577-45FE-9423-284F46D1D657

P31

Q30316581-344A9890-5252-4A09-A37D-730434FFEE94

P356

Q30316581-83A1C17C-D67E-4C74-87D6-00E4407BC689

P407

Q30316581-A1E50A11-B083-43C2-A72E-D66D8D1DDF7C

P433

Q30316581-BE67E254-EE01-411A-B679-D39C5EE8750D

P478

Q30316581-F4C43B46-228C-4D28-82A3-5B873DFA7C6F

P50

Q30316581-B2A240F4-13FE-4BAD-B953-2CB92D5F37E5

P577

Q30316581-2C6D7136-D964-4EC1-9F86-B14037E6BD94

P698

Q30316581-861ACE12-36AD-4C48-9C4F-CB1C83CED7C1

P932

Q30316581-14DCD942-B1AA-446C-BC9E-365AECB27756

P356

JBC.M114.593228

P1433

Journal of Biological Chemistry

P1476

Parvulin 17-catalyzed Tubulin ...... in a Calcium-dependent Manner

@en

P2093

Andreas Schmidt

http://www.w3.org/2001/XMLSchema#string

Annika Manns

http://www.w3.org/2001/XMLSchema#string

Antonia Masch

http://www.w3.org/2001/XMLSchema#string

Bianca Schulze

http://www.w3.org/2001/XMLSchema#string

Christian Lücke

http://www.w3.org/2001/XMLSchema#string

Günther Jahreis

http://www.w3.org/2001/XMLSchema#string

Matthias Weiwad

http://www.w3.org/2001/XMLSchema#string

Noelia Inés Burgardt

http://www.w3.org/2001/XMLSchema#string

Yi-Jan Lin

http://www.w3.org/2001/XMLSchema#string

P2860

Characterization of novel elongated Parvulin isoforms that are ubiquitously expressed in human tissues and originate from alternative transcription initiation.

Function of WW domains as phosphoserine- or phosphothreonine-binding modules

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

The DNA binding parvulin Par17 is targeted to the mitochondrial matrix by a recently evolved prepeptide uniquely present in Hominidae

The N-terminal basic domain of human parvulin hPar14 is responsible for the entry to the nucleus and high-affinity DNA-binding

Bcl-2 regulator FKBP38 is activated by Ca2+/calmodulin.

Small family with key contacts: par14 and par17 parvulin proteins, relatives of pin1, now emerge in biomedical research

NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein

Solution structure of the human parvulin-like peptidyl prolyl cis/trans isomerase, hPar14

P304

16708-16722

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M114.593228

http://www.w3.org/2001/XMLSchema#string

P407

P433

27

http://www.w3.org/2001/XMLSchema#string

P478

290

http://www.w3.org/2001/XMLSchema#string

P50

Alexandra Schutkowski

P577

2015-05-04T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

25940090

http://www.w3.org/2001/XMLSchema#string

P932

4505421

http://www.w3.org/2001/XMLSchema#string